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Sweet entanglements—protein: Glycan interactions in two HIV-inactivating lectin families†
Article first published online: 29 SEP 2012
Copyright © 2012 Wiley Periodicals, Inc.
Special Issue: PDB40: The Protein Data Bank Celebrates its 40th Birthday
Volume 99, Issue 3, pages 196–202, March 2013
How to Cite
Koharudin, L. M. I. and Gronenborn, A. M. (2013), Sweet entanglements—protein: Glycan interactions in two HIV-inactivating lectin families. Biopolymers, 99: 196–202. doi: 10.1002/bip.22106
- Issue published online: 21 DEC 2012
- Article first published online: 29 SEP 2012
- Accepted manuscript online: 22 JUN 2012 11:12PM EST
- Manuscript Accepted: 25 MAY 2012
- Manuscript Received: 15 MAY 2012
- National Institutes of Health. Grant Number: R01GM080642
Structures and sugar binding by members of two lectin families, Cyanovirin-N homolog (CVNH) and Oscillatoria Agardhii agglutinin homolog (OAAH), were determined to elucidate the basis for recognition of high-mannose glycans on the HIV envelope glycoprotein gp120. We solved NMR solution and/or crystal structures for several lectins and delineated their carbohydrate specificity by array screening and direct NMR titrations. Both families recognize different epitopes on high-mannose glycans, namely, Manα(1-2)Man units at the end of the D1 and D3 arms and α3,α6-mannopentaose at the central branch point of Man-8 or Man-9 for CVNH and OAAH lectins, respectively. © 2012 Wiley Periodicals, Inc. Biopolymers 99: 196–202, 2013.